Published June 24, 2010 | Version v1
Journal article

Characterization, crystallization and preliminary X-ray analysis of the adhesive domain of SdrE from Staphylococcus aureus

  • 1. Key Laboratory of Zoonosis, Ministry of Education, Institute of Zoonosis, College of Animal Science and Veterinary Medicine, Jilin University, Changchun 130062 (China)
  • 2. MOE Key Laboratory of Bioinformatics and Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084 (China)
  • 3. Department of Immunology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069 (China)

Description

The adhesive domain of SdrE from Staphylococcus aureus was recombinantly expressed in Escherichia coli and crystallized. X-ray diffraction data were collected to 1.8 Å resolution. The adhesive domain of SdrE from Staphylococcus aureus was recombinantly expressed in Escherichia coli. The purified protein was identified by SDS–PAGE and MALDI–TOF MS. The protein was crystallized using the vapour-diffusion method in hanging-drop mode with PEG 8000 as the primary precipitating agent. X-ray diffraction data were collected to 1.8 Å resolution from a single crystal of the protein. Preliminary X-ray analysis indicated that the crystal belonged to space group P1, with unit-cell parameters a = 40.714, b = 66.355, c = 80.827 Å, α = 111.19, β = 93.99, γ = 104.39°

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309110020907; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2898480

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
66
Journal Issue
Pt 7
Journal Page Range
p. 858-861
ISSN
1744-3091
CODEN
ACSFCL

INIS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2010
Notes
PMCID: PMC2898480; PMID: 20606292; PUBLISHER-ID: hc5099; OAI: oai:pubmedcentral.nih.gov:2898480